We have found that sulfated glycolipids participate in tumor cell adhesion by directly promoting adhesion (Cancer Res 1988;48:3367) and as receptors for thrombospondin on melanoma cells (Cancer Res l988;48:6785). Relatively few of the glycolipids belonging to this class have been characterized. We are purifying novel sulfated glycolipids from several sources including human kidney and meconium and breast and small cell lung carcinoma cell lines. The structures of these glycolipids will be examined using chemical and immunological approaches. Monoclonal antibodies to these will be used to examine the potential of these structures as tumor markers. The molecular basis of binding of adhesive glycoproteins to sulfatide and heparan sulfate proteoglycans are being investigated by identifying sequences in these molecules responsible for binding. Both proteolytic and recombinant fragments of the adhesive proteins are being used to map the active binding domains.